Information on the structure and function of proteins is important for unveiling the biological processes taking place on a molecular level. X-ray crystallography has been successful in determining protein structure, however is not well suited for analyzing hydrogen atoms and water molecules. It has been shown that the thermal neutrons are a far better tool for probing interactions between proteins and water, because they interact directly with light nuclei, not their electron clouds as in case of x-ray diffraction. However, the use of thermal neutrons has been underutilized in this country, partially due to the lack of adequate detectors. Current two-dimensional detector for neutrons do not provide adequate area coverage, spatial resolution, sensitivity, and geometry best suited for the given application. To address these issues, we propose to develop a large area digital imaging detector for thermal neutrons, which offers a better combination of surface coverage, spatial resolution, detection efficiency and dynamic range than is currently possible. The detector is based on an novel, large-area scintillator, tailored for imaging thermal neutrons, coupled tot a digital readout. This thermal neutron imaging system will advance the state-of-the-art of detectors used in macromolecular crystallography and neutron radiography. [unreadable] [unreadable]